MTNA_RAT
ID MTNA_RAT Reviewed; 369 AA.
AC Q5HZE4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein {ECO:0000255|HAMAP-Rule:MF_03119};
GN Name=Mri1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03119};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 1/6. {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_03119}.
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DR EMBL; BC089060; AAH89060.1; -; mRNA.
DR RefSeq; NP_001010947.1; NM_001010947.1.
DR AlphaFoldDB; Q5HZE4; -.
DR SMR; Q5HZE4; -.
DR STRING; 10116.ENSRNOP00000003762; -.
DR iPTMnet; Q5HZE4; -.
DR PhosphoSitePlus; Q5HZE4; -.
DR jPOST; Q5HZE4; -.
DR PaxDb; Q5HZE4; -.
DR PRIDE; Q5HZE4; -.
DR Ensembl; ENSRNOT00000003762; ENSRNOP00000003762; ENSRNOG00000026211.
DR GeneID; 288912; -.
DR KEGG; rno:288912; -.
DR CTD; 84245; -.
DR RGD; 1307789; Mri1.
DR eggNOG; KOG1468; Eukaryota.
DR GeneTree; ENSGT00390000013732; -.
DR HOGENOM; CLU_016218_1_3_1; -.
DR InParanoid; Q5HZE4; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1410886at2759; -.
DR PhylomeDB; Q5HZE4; -.
DR TreeFam; TF300852; -.
DR Reactome; R-RNO-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00874.
DR PRO; PR:Q5HZE4; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000026211; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q5HZE4; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR005251; IF-M1Pi.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Cytoplasm; Isomerase;
KW Methionine biosynthesis; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..369
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000317327"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 168
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV20"
FT MOD_RES 158
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQT1"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 369 AA; 39587 MW; 1163019AB4B5EC64 CRC64;
MRLEAIRYSP GSLQILDQLQ LPEHCHYETL SSVQQAREAI RAMKVRGAPA IALVGCLSLA
VELQAGAGGP GLAALVAFVR DQLSLLVAAR PTAVNMARAA RDLTHMAARE AELEGATEET
VRERVIRFAE DMLEKDLKDN RSIGDLGARH LLEQTNPRGG KVTVLTHCNT GALATAGYGT
ALGVIRSLHE MGRLEHTFCT ETRPYNQGAR LTAFELVYEK IPATLITDSM AAAAMVHQGV
SAVVVGADRV VANGDTANKI GTYQLAIVAK HHGIPFYVAA PSSSCDLRLE TGKEIVIEER
PSQELTDLNG VRIAAQGIRV WNPAFDVTPH ELITGGIITE LGVFAPEELR AALSATIFSE
GQTLDSPQM
